Conformation of poly-L-tyrosine in trimethyl phosphate solution
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چکیده
منابع مشابه
Conformation of poly-L-glutamate is independent of ionic strength.
CD and UV resonance Raman measurements surprisingly find that the charge screening of even 2 M concentrations of NaCl and KCl does not alter the unfolded PPII and 2.5(1)-helix conformations of poly-L-glutamate. These salts appear to be excluded from the region between the side chain charges and the peptide backbone. Furthermore, no direct ion pairing occurs between these salts and the side chai...
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A large-scale fully-atomistic molecular dynamics simulation of poly-l-glutamate demonstrates that a small amount of sodium chloride switches the preferred conformation from an extended conformation to a compact alpha-helix.
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ژورنال
عنوان ژورنال: Biopolymers
سال: 1971
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.360100219